Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Algal and fungal genes and their uses for taurine biosynthesis in cells

a technology of taurine and genes, applied in the field of recombinant production of taurine, can solve the problems of never providing validation, never divulging the sequences of genes or the sequences of corresponding peptides, etc., and achieves the effects of improving the characteristics of food, increasing the level of sulfur-containing compounds, and increasing nutritional valu

Active Publication Date: 2021-08-03
PLANT SENSORY SYST
View PDF4 Cites 0 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

This approach increases taurine levels in transgenic organisms, enhancing their nutritional value, growth characteristics, and therapeutic potential, while providing a sustainable method for taurine production and application in food, feed, and pharmaceuticals.

Problems solved by technology

However, they never disclose the sequences of the genes or the sequences of the corresponding peptides.
Nor do they provide validation through genetic (knock-out or complementation) or biochemical means of the function of the genes or their corresponding peptides.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Algal and fungal genes and their uses for taurine biosynthesis in cells
  • Algal and fungal genes and their uses for taurine biosynthesis in cells

Examples

Experimental program
Comparison scheme
Effect test

example 1

Development of a Transgenic Plant that Constitutively Expresses CDOL with the Native Transit Peptide and Constitutively Expresses SADL with the Native Transit Peptide in Tandem with Independent Promoters

[0471]Step 1: Use chemical synthesis to make a DNA construct that contains a constitutive promoter, 35S, fused with the nucleotide sequence for CDOL gene (SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, or SEQ ID NO:4) and a NOS terminator. Clone the DNA construct into a binary vector, such as pCambia1300, pCambia2300, or pCambia3200.

[0472]The CDOL gene is as follows:[0473]a. Derived from SEQ ID NO:1, optimized for expression in Arabidopsis or soybean (dicots) or corn (a monocot), and encoding a CDOL peptide from Chlamydomonas reinhardtii (SEQ ID NO:5); or[0474]b. Derived from SEQ ID NO:2, optimized for expression in Arabidopsis or soybean (dicots) or corn (a monocot), and encoding a CDOL peptide from Guillardia theta (SEQ ID NO:6); or[0475]c. Derived from SEQ ID NO:3, optimized for expressio...

example 2

Development of a Transgenic Plant that Constitutively Expresses CDOL with a Plant Plastid Transit Peptide and Constitutively Expresses SADL Protein with a Plant Plastid Transit Peptide in Tandem with Independent Promoters

[0485]Step 1: Use chemical synthesis to make a DNA construct that contains a constitutive promoter, 35S, fused with the nucleotide sequence for a plastid transit peptide (SEQ ID NO:21), truncated CDOL gene (SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, or SEQ ID NO:4) and a NOS terminator. Clone the DNA construct into a binary vector, such as pCambia1300, pCambia2300, or pCambia3200.

[0486]The nucleotide sequence for the plastid transit peptide (SEQ ID NO:21) encodes the peptide SEQ ID NO:22.

[0487]The CDOL gene is as follows:[0488]a. Derived from SEQ ID NO:1 by removing nucleotides 1 through 159 (corresponding to the native transit peptide), optimized for expression in Arabidopsis or soybean (dicots) or corn (a monocot), and encoding a CDOL peptide from Chlamydomonas reinha...

example 3

Development of a Transgenic Plant that Constitutively Expresses CDOL with the Native Plastid Transit Peptide and Constitutively Expresses CS / PLP-DC with the Native Transit Peptide in Tandem with Independent Promotes

[0501]Step 1: Use chemical synthesis to make a DNA construct that contains a constitutive promoter, 35S, fused with the nucleotide sequence for CDOL gene (SEQ ID NO:1, SEQ ID NO:2, SEQ ID NO:3, or SEQ ID NO:4) and a NOS terminator. Clone the DNA construct into a binary vector, such as pCambia1300, pCambia2300, or pCambia3200.

[0502]The CDOL gene is as follows:[0503]a. Derived from SEQ ID NO:1, optimized for expression in Arabidopsis or soybean (dicots) or corn (a monocot), and encoding a CDOL peptide from Chlamydomonas reinhardtii (SEQ ID NO:5); or[0504]b. Derived from SEQ ID NO:2, optimized for expression in Arabidopsis or soybean (dicots) or corn (a monocot), and encoding a CDOL peptide from Guillardia theta (SEQ ID NO:6); or[0505]c. Derived from SEQ ID NO:3, optimized f...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
temperatureaaaaaaaaaa
temperatureaaaaaaaaaa
pHaaaaaaaaaa
Login to View More

Abstract

The present invention describes an approach to produce taurine or increase hypotaurine or taurine production in prokaryotes or eukaryotes. More particularly, the invention relates to genetic transformation of organisms with algal, microalgal or fungal genes that encode proteins that pool catalyze the conversion of sulfur-containing compounds such as sulfate or cysteine to taurine. The invention describes methods for the use of polynucleotides for cysteine dioxygenase-like (CDOL), sulfinoalanine decarboxylase-like (SADL), cysteine sulfate / decarboxylase or a portion of the cysteine synthetase / PLP decarboxylase (partCS / PLP-DC) polypeptide in bacteria, alga, yeast, or plants to produce taurine or increase hypotaurine or taurine. The preferred embodiment of the invention is in plants but other organisms may be used. Taurine production or increased levels of hypoataurine or taurine in plants could be used as nutraceutical, pharmaceutical, or therapeutic compounds or as a supplement in animal feed or for animal feed or as an enhancer for plant growth or yield.

Description

CROSS-REFERENCE TO RELATED APPLICATION[0001]This application is a 35 U.S.C. § 371 National Stage of International Patent Application No. PCT / US2016 / 026465, filed 7 Apr. 2016, designating the United States, which is incorporated herein by reference in its entirety.SEQUENCE SUBMISSION[0002]The present application is being filed along with a Sequence Listing in electronic format. The Sequence Listing is 3834117PCT SequenceListing.txt, created on 5 Apr. 2016 and is 69 kb in size. The information in the electronic format of the Sequence Listing is incorporated herein by reference in their entiretyFIELD OF THE INVENTION[0003]The present invention is in the field of recombinant production of taurine. The present invention includes the production of taurine in bacteria, microbes, yeast, fungi, plants and animals to increase taurine levels. The invention also relates to methods to increase taurine levels in the cells and to use the said cells or extracts, the plant or plant organs that conta...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
Patent Type & Authority Patents(United States)
IPC IPC(8): C12N9/10C12N9/02C12N15/74C12N15/82A23K50/80C12N15/52
CPCC12Y113/1102A23K50/80C12N9/0069C12N9/1085C12N15/52C12N15/74C12N15/8257A23V2250/0644C12Y205/01047C12P13/001A61K31/185Y02A50/30
Inventor TURANO, FRANK J.
Owner PLANT SENSORY SYST
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com